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Electron transfer and folding studies in designed three-helix bundle peptides :The effects of main chain hydrogen bonds.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Electron transfer and folding studies in designed three-helix bundle peptides :
Reminder of title:	The effects of main chain hydrogen bonds.
Author:	Zheng, Yongjian.
Description:	120 p.
Notes:	Adviser: George McLendon.
Notes:	Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0703.
Contained By:	Dissertation Abstracts International64-02B.
Subject:	Chemistry, Biochemistry.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3080044
ISBN:	0496279211

Electron transfer and folding studies in designed three-helix bundle peptides :The effects of main chain hydrogen bonds.
Zheng, Yongjian.

Electron transfer and folding studies in designed three-helix bundle peptides :The effects of main chain hydrogen bonds. [electronic resource] - 120 p.

Adviser: George McLendon.

Thesis (Ph.D.)--Princeton University, 2003.

Electron transfer reactions play a crucial role in many physiological processes involving energy generation and utilization. Many such reactions taking place in biological systems are long-range interactions with electron donor and acceptor separated well beyond collisional distance. They require proteins as intervening media to couple the donor and acceptor and provide a matrix for electron tunneling.

ISBN: 0496279211Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Electron transfer and folding studies in designed three-helix bundle peptides :The effects of main chain hydrogen bonds.
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245 1 0 $a Electron transfer and folding studies in designed three-helix bundle peptides : $b The effects of main chain hydrogen bonds. $h [electronic resource]
300 $a 120 p.
500 $a Adviser: George McLendon.
500 $a Source: Dissertation Abstracts International, Volume: 64-02, Section: B, page: 0703.
502 $a Thesis (Ph.D.)--Princeton University, 2003.
520 # $a Electron transfer reactions play a crucial role in many physiological processes involving energy generation and utilization. Many such reactions taking place in biological systems are long-range interactions with electron donor and acceptor separated well beyond collisional distance. They require proteins as intervening media to couple the donor and acceptor and provide a matrix for electron tunneling.
520 # $a In the research presented here, a novel method was developed to synthetically replace a backbone peptide linkage with an ester isostere in a 20 amino acid peptide, deleting one of the main-chain hydrogen bonds. The hydrogen bond intact construct and three hydrogen bond deleted peptides were incorporated into a metal-ion assisted three-helix bundle system. Chemical denaturation and electron transfer studies were carried out in these peptides to elucidate the role of these hydrogen bonds in protein folding stability and electron transfer pathways. Hydrogen bonds in the three-helix bundle construct contribute as much as 1.1 kcal/mol to the overall folding free energy. Also, hydrogen bonds at different locations in the helical structure have different influences on protein stability.
520 # $a Pathway model predicts significantly different electron transfer rates by calculating the electronic coupling factors of hydrogen bond deleted and "wild type" peptides. However, the peptides under investigation exhibit similar electron transfer rates as measured by pulse radiolysis experiments, which are in good agreement with that predicted by simple distance model, indicating pathway independent characteristics of electron transfer in the three-helix bundle system. Pathway model is successful in explaining the difference in beta value for alpha-helices and beta-strands, but it is not evident from the observations in our experiments that electron transfer is strongly pathway dependent, at least not for intervening matrices that have the same alpha-helical structure.
520 # $a The rates of electron transfer are dependent on the donor-acceptor distance. Different protein structures between the redox centers also have different effects in facilitating electron transfer. Hydrogen bonds can act like bridges amongst the tortuous protein backbone and greatly shorten the electron transfer pathway. Hydrogen bonds have a significant impact on many other aspects of protein chemistry, such as protein structure, folding and stability.
590 $a School code: 0181.
650 # 0 $a Chemistry, Biochemistry. $3 226900
650 # 0 $a Chemistry, Organic. $3 193634
650 # 0 $a Biophysics, General. $3 226901
710 0 # $a Princeton University. $3 212488
773 0 # $g 64-02B. $t Dissertation Abstracts International
790 $a 0181
790 1 0 $a McLendon, George, $e advisor
791 $a Ph.D.
792 $a 2003
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